- J. Martin Scholtz
- Professor of Molecular and Cellular Medicine and of Biochemistry and Biophysics; Associate Vice President for Research at Texas A&M
- Undergraduate Education
- B.S. University of Nebraska, Lincoln (1984)
- Graduate Education
- Ph.D. University of California, Berkeley (1989)
- Postdoc. Stanford University (1989-93)
- Joined Texas A&M in 1993
Helix Formation in Protein Folding and Stability
We are interested in the problem of protein folding – a description of the mechanism by which a protein adopts a given three dimensional structure using only the information encoded in the primary sequence of amino acids. We are currently testing the idea that protein folding and stability can be described in a hierarchical fashion: building stability and structure from the primary sequence through secondary structure to the tertiary structure of proteins. Toward this end, our efforts have concentrated on the role helix stability plays in governing protein folding and stability in several model proteins.
A variety of biochemical and biophysical techniques are employed to explore the energetics of helix formation in model peptides, in peptides derived from helical structures of proteins and in intact proteins. Our goal is to determine quantitative rules for helix formation in proteins, realizing that these rules may serve as useful tools to predict protein structure from sequence.
Recently, we have initiated a project on transmembrane helix formation with the realization that the “rules” for helix formation in membranes are likely to be very different than those for water-soluble proteins. Again, our goal is to formulate energetic rules for transmembrane helix formation that will aid in prediction and future protein design strategies.
Nick Pace, C, Scholtz, JM, Grimsley, GR. Forces stabilizing proteins. FEBS Lett. 2014;588 (14):2177-84.
Pace, CN, Fu, H, Lee Fryar, K, Landua, J, Trevino, SR, Schell, D et al.. Contribution of hydrogen bonds to protein stability. Protein Sci. 2014;23 (5):652-61.
Grimsley, GR, Trevino, SR, Thurlkill, RL, Scholtz, JM. Determining the conformational stability of a protein from urea and thermal unfolding curves. Curr Protoc Protein Sci. 2013;Chapter 28 :Unit28.4.
Kramer, RM, Shende, VR, Motl, N, Pace, CN, Scholtz, JM. Toward a molecular understanding of protein solubility: increased negative surface charge correlates with increased solubility. Biophys. J. 2012;102 (8):1907-15.
Pace, CN, Fu, H, Fryar, KL, Landua, J, Trevino, SR, Shirley, BA et al.. Contribution of hydrophobic interactions to protein stability. J. Mol. Biol. 2011;408 (3):514-28.
Fu, H, Grimsley, G, Scholtz, JM, Pace, CN. Increasing protein stability: importance of DeltaC(p) and the denatured state. Protein Sci. 2010;19 (5):1044-52.
Nick Pace, C, Huyghues-Despointes, BM, Fu, H, Takano, K, Scholtz, JM, Grimsley, GR et al.. Urea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteins. Protein Sci. 2010;19 (5):929-43.
McCluggage, LK, Scholtz, JM. Golimumab: a tumor necrosis factor alpha inhibitor for the treatment of rheumatoid arthritis. Ann Pharmacother. 2010;44 (1):135-44.
McLean, JR, McLean, JA, Wu, Z, Becker, C, Pérez, LM, Pace, CN et al.. Factors that influence helical preferences for singly charged gas-phase peptide ions: the effects of multiple potential charge-carrying sites. J Phys Chem B. 2010;114 (2):809-16.
Cho, Y, Sagle, LB, Iimura, S, Zhang, Y, Kherb, J, Chilkoti, A et al.. Hydrogen bonding of beta-turn structure is stabilized in D(2)O. J. Am. Chem. Soc. 2009;131 (42):15188-93.